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HpBoRB, a helminth-derived CCP domain protein which binds RELMβ.

Vivien Shek1, Abhishek Jamwal2, Danielle J Smyth1

  • 1Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee, the United Kingdom of Great Britain and Northern Ireland.

International Journal for Parasitology
|September 26, 2025
PubMed
Summary

The intestinal nematode Heligmosomoides polygyrus bakeri (Hpb) secretes proteins that interact with host immunity. A newly identified Hpb protein, HpBoRB, binds to the anti-helminth protein resistin-like molecule beta (RELMβ), potentially evading host defenses.

Keywords:
AVEXISComplement Control ProteinHeligmosomoides polygyrus bakeriImmunomodulationProtein–protein interactionRELMβ

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Area of Science:

  • Parasitology
  • Immunology
  • Molecular Biology

Background:

  • Helminth infections establish by releasing immunomodulatory proteins to evade host immunity.
  • The intestinal nematode Heligmosomoides polygyrus bakeri (Hpb) secretes numerous immunomodulatory proteins, many containing Complement Control Protein (CCP) domains.

Purpose of the Study:

  • To identify novel Hpb-secreted proteins with immunomodulatory functions.
  • To investigate potential interactions between Hpb proteins and host immune molecules.

Main Methods:

  • Genome-wide identification of CCP domain-containing proteins in Hpb.
  • Screening of cloned Hpb proteins for interactions with host immune proteins using Avidity-based Extracellular Interaction Screening (AVEXIS).
  • Validation of interactions using ELISA, competition assays, size exclusion chromatography, and surface plasmon resonance.

Main Results:

  • Confirmed known interactions between Hpb proteins (HpBARI, TGM1) and their targets (ST2, TGFBR2).
  • Discovered a novel interaction between a 2 CCP domain Hpb protein, named HpBoRB, and mouse resistin-like molecule beta (RELMβ).
  • HpBoRB exhibits specific, heat-labile binding to RELMβ with subnanomolar affinity.

Conclusions:

  • Hpb secretes a diverse repertoire of CCP domain proteins, including novel interactors with host immune molecules.
  • The newly identified HpBoRB protein may interfere with the anti-helminth function of RELMβ, contributing to parasite persistence.
  • This study expands the understanding of host-parasite interactions mediated by secreted Hpb proteins.